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    A bimodal pattern of InsP(3)-evoked elementary Ca(2+) signals in pancreatic acinar cells

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    Authors
    Fogarty, Kevin E.
    Kidd, Jackie F.
    Tuft, Richard A.
    Thorn, Peter
    UMass Chan Affiliations
    Biomedical Imaging Group
    Document Type
    Journal Article
    Publication Date
    2000-04-25
    Keywords
    Animals
    Biophysics
    Calcium Channels
    Calcium Signaling
    Female
    Inositol 1,4,5-Trisphosphate
    Inositol 1,4,5-Trisphosphate Receptors
    Male
    Mice
    Microscopy, Fluorescence
    Oocytes
    Pancreas
    Patch-Clamp Techniques
    Protein Isoforms
    Receptors, Cytoplasmic and Nuclear
    Xenopus
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1300821/pdf/10777728.pdf
    Abstract
    InsP(3)-evoked elementary Ca(2+) release events have been postulated to play a role in providing the building blocks of larger Ca(2+) signals. In pancreatic acinar cells, low concentrations of acetylcholine or the injection of low concentrations of InsP(3) elicit a train of spatially localized Ca(2+) spikes. In this study we have quantified these responses and compared the Ca(2+) signals to the elementary events shown in Xenopus oocytes. The results demonstrate, at the same concentrations of InsP(3), Ca(2+) signals consisting of one population of small transient Ca(2+) release events and a second distinct population of larger Ca(2+) spikes. The signal mass amplitudes of both types of events are within the range of amplitudes for the elementary events in Xenopus oocytes. However, the bimodal Ca(2+) distribution of Ca(2+) responses we observe is not consistent with the continuum of event sizes seen in Xenopus. We conclude that the two types of InsP(3)-dependent events in acinar cells are both elementary Ca(2+) signals, which are independent of one another. Our data indicate a complexity to the organization of the Ca(2+) release apparatus in acinar cells, which might result from the presence of multiple InsP(3) receptor isoforms, and is likely to be important in the physiology of these cells.
    Source
    Biophys J. 2000 May;78(5):2298-306.
    DOI
    10.1016/S0006-3495(00)76776-2
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/39897
    PubMed ID
    10777728
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1016/S0006-3495(00)76776-2
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